Abstract
We report a detailed dynamical study on a hydrated protein, Lysozyme comparing its dynamical features with those obtained in the case of aqueous solutions whose solute is a synthetic polymer, Poly(ethylene glycol), PEG600. The noteworthy feature of this kind of analysis is that it is yet reasonable to apply the same theoretical model to the experimental data, even if the complexity of the solute molecules, in passing from the polymer to the protein, increases dramatically. The experimental measurements performed by Incoherent Quasi Elastic Neutron Scattering technique (IQENS) were carried out by using hydration conditions in H 2O and D 2O in order to clearly evaluate the different contributions of the protein/polymer matrix from that of hydration water. A clear slowing down in the dynamics of the latter with respect to the bulk water is revealed in both the cases.
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